Recently we have shown that a very small anomalous diffraction signal (less than 0.5% of the total) of sulfur atoms, intrinsically present in all proteins can be succssfully used to solve crystal structures of proteins. This approach may become a routine technique in the practice olf macromolecular crystallography. The diffraction data to extremely high resolution of 0.65 angstrom were measured using synchrotron radiation, and the refined model reveals the unprecedented structgural details of the molecule of lysozyme. The structure of the single-stranded DNA-binding protein from T. aquaticus was solved showing that the two-OB domain subunit of this protein forms oligomers analogous to the more typical, single-domain SSBs from other bacteria. The crystal structure of the uropathogenic E. coli invasin DraD was solved and revealed the unusual self-complementing mwechanism of aggregation, utilized by the becteria in formation of invasive fibrils. We participated in several collaborative structural projects on various biologically important proteins, such as Nervy homology two domain or the argonaute protein.